CAZyme Information: SMAC_06939-t26_1-p1

Basic Information

• Species: Sordaria macrospora
• Lineage: Ascomycota; Sordariomycetes; ; Sordariaceae; Sordaria; Sordaria macrospora
• CAZyme ID: SMAC_06939-t26_1-p1
• CAZy Family: GH43|CBM91
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1302		141463.82	4.7338

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Smacrosporak-hell	11311	771870	484	10827

• Gene Location: location=NW_003546142:253782-257973(-)

Full Sequence      

MGRPSATSFGKLVSSLFASWAVVSDVIGGIANAAALASPSDALESPSPFFSQLRRCPAAC
SNCQSPEEWTVYSTFDRLKHCNETLLIDFSIHIPLDTPDIVVRACSTAGNAPVNPAVAEI
VTSQSLLDGEDEGGFSTAAAATSDVCVEASNSNTVEAELAWRAGEHSSVSGDRDDVLLAA
QEVQRNLQTVDGCDETIIFGYSNEVVVGVFAGSKVDKASVASLINAQFLAKDRRETVNPE
SVSSFLQICGKGRNADYTVGVAAGNIASVQAAVLSWSKAVCVDTSGATKVERQSVQIKTR
PYKKPVSQSIYSNSTALQPRLYLADCTTVKVVSGDICQTLAEDKCGITLTKFKSYNNLTD
SGCNSLVVGQAVCCTIGPLPDIRPKPKANGECASYIIKSGNSCSSIAAANGLTVDDLDKF
NKKTWQWNGCDLILPGVKICLSTGDPPLPAPVSNAICGPTKPGTTRPSDKSKELADLNPC
PLNACCNIWGQCGVTDEFCKITTSKSGGDTGCISNCGMEIIKGAEPPAFYRTVGYFEAWN
KERPCLRMDASQIDAENIQYMDQFNKFKALKNIKRIVAFGGWAFSTEVATYARFREGVQE
ANREVLATKIVAFVKQHGLDGVDFDWEYPGAGSPDIPDIPPGTPDDGPNYAAFLKLVKQK
LRAVNTNLTLSIAAPAGYWFLRAFHPLDKMAESLDYIVYMTYDLHGQWDYGGPWASSGCP
EGNCLRSHVNWTETVSALTLITKTGVPASKILFGIGSYGRSFQMTDPGCRDVNCHFVGPQ
SGATPGRCTQTAGYISNAEINDITYIATPGVKTWSDQESLTNFVVYNGDQWVAYSGGLFT
WRREEWARIWNFGGTSEWAIDLQEYHYPVYGDELEEGMELDDEGLWDAPKAEYCEPKSFN
ELDDIPDGQTAKCGAIYVLETLANMLKADLATYKDILSNSYDKKFKVYAEVVAELAPDQV
QDFLLEHGNDYFTCVVNEIFYCAAWCGREWGLGDSYCRYITIDTCQASHGGPGVTFGNVT
EPCPPDYSKRGAGDYPALRDQRTVYWSLRPDKADSFYKDLLNATGIDKNDTVINWHTKEQ
HKRLECREFPRCLDHGEWDWGPTTKGNYSVSDVTNPKEIIEKLLDTASGLEHELRIAAQE
IYAGTSEVMYSDMVDSTGLPVLMIRQAVESMKQVVEAADEINKQRKKQMILFFLMAFLFL
IPIGGSAIGAIGGLANLGRIVAMAGEAAMIGLDIYSVTQDPSQAPFLIFGNILSVGALKN
PVKMNTAAAARRAMGPDDISRLGEIVTKGLGKIATVVSKVCR

Enzyme Prediction     

EC	3.2.1.14:3

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH18	530	862	8.8e-48	0.9324324324324325

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
119357	GH18_zymocin_alpha	3.75e-173	531	863	1	345	Zymocin, alpha subunit. Zymocin is a heterotrimeric enzyme that inhibits yeast cell cycle progression. The zymocin alpha subunit has a chitinase activity that is essential for holoenzyme action from the cell exterior while the gamma subunit contains the intracellular toxin responsible for G1 phase cell cycle arrest. The zymocin alpha and beta subunits are thought to act from the cell's exterior by docking to the cell wall-associated chitin, thus mediating gamma-toxin translocation. The alpha subunit has an eight-stranded TIM barrel fold similar to that of family 18 glycosyl hydrolases such as hevamine, chitolectin, and chitobiase.
214753	Glyco_18	6.25e-55	531	862	1	333	Glyco_18 domain.
395573	Glyco_hydro_18	1.69e-49	531	841	1	302	Glycosyl hydrolases family 18.
119351	GH18_chitolectin_chitotriosidase	7.58e-47	564	866	58	344	This conserved domain family includes a large number of catalytically inactive chitinase-like lectins (chitolectins) including YKL-39, YKL-40 (HCGP39), YM1, oviductin, and AMCase (acidic mammalian chitinase), as well as catalytically active chitotriosidases. The conserved domain is an eight-stranded alpha/beta barrel fold belonging to the family 18 glycosyl hydrolases. The fold has a pronounced active-site cleft at the C-terminal end of the beta-barrel. The chitolectins lack a key active site glutamate (the proton donor required for hydrolytic activity) but retain highly conserved residues involved in oligosaccharide binding. Chitotriosidase is a chitinolytic enzyme expressed in maturing macrophages, which suggests that it plays a part in antimicrobial defense. Chitotriosidase hydrolyzes chitotriose, as well as colloidal chitin to yield chitobiose and is therefore considered an exochitinase. Chitotriosidase occurs in two major forms, the large form being converted to the small form by either RNA or post-translational processing. Although the small form, containing the chitinase domain alone, is sufficient for the chitinolytic activity, the additional C-terminal chitin-binding domain of the large form plays a role in processing colloidal chitin. The chitotriosidase gene is nonessential in humans, as about 35% of the population are heterozygous and 6% homozygous for an inactivated form of the gene. HCGP39 is a 39-kDa human cartilage glycoprotein thought to play a role in connective tissue remodeling and defense against pathogens.
119365	GH18_chitinase	2.28e-40	554	763	62	267	The GH18 (glycosyl hydrolases, family 18) type II chitinases hydrolyze chitin, an abundant polymer of N-acetylglucosamine and have been identified in bacteria, fungi, insects, plants, viruses, and protozoan parasites. The structure of this domain is an eight-stranded alpha/beta barrel with a pronounced active-site cleft at the C-terminal end of the beta-barrel.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QGA18426.1|CBM18|CBM50|GH18	2.72e-268	49	1296	23	1305
UKZ79373.1|CBM18|CBM50|GH18	1.07e-265	53	1299	30	1279
UPK95779.1|CBM18|CBM50|GH18	1.83e-248	56	1274	33	1227
EGX48217.1|CBM18|CBM50|GH18	1.33e-247	49	1284	28	1216
CBF71201.1|CBM18|GH18	7.74e-243	43	1294	40	1225

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5WUP_A	8.98e-31	562	871	155	446	Crystal structure of a insect group III chitinase (CAD1) from Ostrinia furnacalis [Ostrinia furnacalis],5WV9_A Crystal structure of a insect group III chitinase complex with (GlcNAc)6 (CAD1-(GlcNAc)6) from Ostrinia furnacalis [Ostrinia furnacalis]
3FXY_A	8.21e-30	564	865	56	346	Acidic Mammalian Chinase, Catalytic Domain [Homo sapiens],3FXY_B Acidic Mammalian Chinase, Catalytic Domain [Homo sapiens],3FXY_C Acidic Mammalian Chinase, Catalytic Domain [Homo sapiens],3FXY_D Acidic Mammalian Chinase, Catalytic Domain [Homo sapiens],3FY1_A The Acidic Mammalian Chitinase catalytic domain in complex with methylallosamidin [Homo sapiens],3FY1_B The Acidic Mammalian Chitinase catalytic domain in complex with methylallosamidin [Homo sapiens],3RM4_A AMCase in complex with Compound 1 [Homo sapiens],3RM4_B AMCase in complex with Compound 1 [Homo sapiens],3RM8_A AMCase in complex with Compound 2 [Homo sapiens],3RM8_B AMCase in complex with Compound 2 [Homo sapiens],3RM9_A AMCase in complex with Compound 3 [Homo sapiens],3RM9_B AMCase in complex with Compound 3 [Homo sapiens],3RME_A AMCase in complex with Compound 5 [Homo sapiens],3RME_B AMCase in complex with Compound 5 [Homo sapiens]
2YBT_A	8.63e-30	564	865	60	350	Crystal structure of human acidic chitinase in complex with bisdionin C [Homo sapiens],2YBT_B Crystal structure of human acidic chitinase in complex with bisdionin C [Homo sapiens],2YBT_C Crystal structure of human acidic chitinase in complex with bisdionin C [Homo sapiens],2YBT_D Crystal structure of human acidic chitinase in complex with bisdionin C [Homo sapiens],2YBT_E Crystal structure of human acidic chitinase in complex with bisdionin C [Homo sapiens],2YBT_F Crystal structure of human acidic chitinase in complex with bisdionin C [Homo sapiens],2YBU_A Crystal structure of human acidic chitinase in complex with bisdionin F [Homo sapiens],2YBU_B Crystal structure of human acidic chitinase in complex with bisdionin F [Homo sapiens],2YBU_C Crystal structure of human acidic chitinase in complex with bisdionin F [Homo sapiens],2YBU_D Crystal structure of human acidic chitinase in complex with bisdionin F [Homo sapiens],2YBU_E Crystal structure of human acidic chitinase in complex with bisdionin F [Homo sapiens],2YBU_F Crystal structure of human acidic chitinase in complex with bisdionin F [Homo sapiens]
5WV8_A	9.40e-30	562	871	155	446	Crystal structure of a mutant insect group III chitinase (CAD1-E217L) from Ostrinia furnacalis [Ostrinia furnacalis],5WVB_A Crystal structure of a mutant insect group III chitinase complex with (GlcNAc)6 (CAD1-E217L-(GlcNAc)6) from Ostrinia furnacalis [Ostrinia furnacalis]
1HKK_A	4.21e-28	563	865	58	344	High resoultion crystal structure of human chitinase in complex with allosamidin [Homo sapiens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P09805|KTXA_KLULA	9.62e-81	343	861	206	710	Killer toxin subunits alpha/beta OS=Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) OX=284590 PE=1 SV=1
sp|Q6RY07|CHIA_RAT	1.50e-32	517	865	9	367	Acidic mammalian chitinase OS=Rattus norvegicus OX=10116 GN=Chia PE=2 SV=1
sp|Q95M17|CHIA_BOVIN	8.68e-32	517	865	9	367	Acidic mammalian chitinase OS=Bos taurus OX=9913 GN=CHIA PE=1 SV=1
sp|Q91XA9|CHIA_MOUSE	3.86e-31	517	865	9	367	Acidic mammalian chitinase OS=Mus musculus OX=10090 GN=Chia PE=1 SV=2
sp|Q9BZP6|CHIA_HUMAN	4.47e-29	517	865	9	367	Acidic mammalian chitinase OS=Homo sapiens OX=9606 GN=CHIA PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.819748	0.180254

TMHMM  Annotations     

Start	End
1192	1214